Quantitative aspects of binding of canine serum immunoglobulins of Staphylococcus aureus protein A.
Quantitative interactions of Staphylococcus aureus protein A (SPA) and canine immunoglobulins (Ig) are described. The S aureus Cowan strain I bound canine IgG, IgM, and IgA, whereas binding was not observed with the SPA-negative Wood 46 strain of S aureus. In a quantitative adsorption experiment, the results indicated that IgA, though present in the lowest amounts in the samples, appeared to be substantially bound by SPA. Adsorption of sera with SPA-negative Wood strain bacteria resulted in nonspecific protein losses in supernatants of 0% to 15%.
D000327:Adsorption; D000818:Animals; D001666:Binding Sites, Antibody; D004285:Dogs / Q000276:immunology*; D005856:Germ-Free Life; D007106:Immune Sera; D005779:Immunodiffusion / Q000662:veterinary; D007122:Immunoelectrophoresis; D007070:Immunoglobulin A / Q000276:immunology; D007074:Immunoglobulin G / Q000276:immunology; D007075:Immunoglobulin M / Q000276:immunology; D007136:Immunoglobulins / Q000276:immunology*; D013205:Staphylococcal Protein A / Q000276:immunology*
D007106:Immune Sera; D007070:Immunoglobulin A; D007074:Immunoglobulin G; D007075:Immunoglobulin M; D007136:Immunoglobulins; D013205:Staphylococcal Protein A